Phospholipase C-gamma 1 (PLCG1) plays a pivotal role in angiogenesis and VEGFR2 signal transduction. VEGFR2-mediated activation of PLCG1 in certain endothelial cellular backgrounds is suggested to stimulate cell proliferation and in other endothelial cells to stimulate differentiation and tubulogenesis (Rahimi 2006). Phosphorylated tyrosine 1175 of VEGFR2 provides the binding site for PLCG1, SHC-transforming protein 2 (SHC2/SCK) and SH2 domain-containing adapter protein B (SHB) (Takahashi et al. 2001). Binding of PLCG1 activates protein kinase C (PKC) and this in-turn stimulates mitogen-activated protein (MAP) kinase (MAPK)-dependent pathway and cell proliferation (McLaughlin & Vries 2001).